2qo3: Difference between revisions

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-[[Image:2qo3.png|left|200px]]
-<!--
+==Crystal Structure of [KS3][AT3] didomain from module 3 of 6-deoxyerthronolide B synthase==
-The line below this paragraph, containing "STRUCTURE_2qo3", creates the "Structure Box" on the page.
+<StructureSection load='2qo3' size='340' side='right'caption='[[2qo3]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2qo3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharopolyspora_erythraea Saccharopolyspora erythraea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QO3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QO3 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.59&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CER:(2S,+3R)-3-HYDROXY-4-OXO-7,10-TRANS,TRANS-DODECADIENAMIDE'>CER</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
-{{STRUCTURE_2qo3|  PDB=2qo3  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qo3 OCA], [https://pdbe.org/2qo3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qo3 RCSB], [https://www.ebi.ac.uk/pdbsum/2qo3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qo3 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ERYA2_SACER ERYA2_SACER]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qo/2qo3_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qo3 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+We report the 2.6 A X-ray crystal structure of a 190 kDa homodimeric fragment from module 3 of the 6-deoxyerthronolide B synthase covalently bound to the inhibitor cerulenin. The structure shows two well-organized interdomain linker regions in addition to the full-length ketosynthase (KS) and acyltransferase (AT) domains. Analysis of the substrate-binding site of the KS domain suggests that a loop region at the homodimer interface influences KS substrate specificity. We also describe a model for the interaction of the catalytic domains with the acyl carrier protein (ACP) domain. The ACP is proposed to dock within a deep cleft between the KS and AT domains, with interactions that span both the KS homodimer and AT domain. In conjunction with other recent data, our results provide atomic resolution pictures of several catalytically relevant protein interactions in this remarkable family of modular megasynthases.
-===Crystal Structure of [KS3][AT3] didomain from module 3 of 6-deoxyerthronolide B synthase===
+Structural and mechanistic analysis of protein interactions in module 3 of the 6-deoxyerythronolide B synthase.,Tang Y, Chen AY, Kim CY, Cane DE, Khosla C Chem Biol. 2007 Aug;14(8):931-43. PMID:17719492<ref>PMID:17719492</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2qo3" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_17719492}}, adds the Publication Abstract to the page
+*[[6-deoxyerythronolide B synthase 3D structures|6-deoxyerythronolide B synthase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 17719492 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_17719492}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-[[2qo3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharopolyspora_erythraea Saccharopolyspora erythraea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QO3 OCA].
-==Reference==
-<ref group="xtra">PMID:17719492</ref><ref group="xtra">PMID:17656315</ref><ref group="xtra">PMID:16844787</ref><ref group="xtra">PMID:15518537</ref><references group="xtra"/>
-[[Category: 6-deoxyerythronolide-B synthase]]
 [[Category: Saccharopolyspora erythraea]]
-[[Category: Cane, E D.]]
+[[Category: Cane ED]]
-[[Category: Chen, Y A.]]
+[[Category: Chen YA]]
-[[Category: Khosla, C.]]
+[[Category: Khosla C]]
-[[Category: Kim, C Y.]]
+[[Category: Kim CY]]
-[[Category: Tang, Y.]]
+[[Category: Tang Y]]
-[[Category: Acyltransferase]]
-[[Category: Ketosynthase]]
-[[Category: Phosphopantetheine]]